Osteonectin, bone proteoglycan, and phosphophoryn defects in a form of bovine osteogenesis imperfecta
| Autor: | Kathleen M. Conn, K G Thompson, H Shimokawa, J B Cruz, G R Hawkins, Larry W. Fisher, John D. Termine, M A Drum, Pamela Gehron Robey |
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| Rok vydání: | 1984 |
| Předmět: |
Bone sialoprotein
medicine.medical_specialty Cattle Diseases Matrix (biology) Bone and Bones chemistry.chemical_compound stomatognathic system Reference Values Internal medicine medicine Dentin Animals Osteonectin Amino Acids Multidisciplinary Viral matrix protein biology Anatomy Osteogenesis Imperfecta Phosphoproteins medicine.disease Molecular Weight stomatognathic diseases Hydroxylysine Endocrinology medicine.anatomical_structure chemistry Proteoglycan Osteogenesis imperfecta biology.protein Cattle Proteoglycans Collagen Carrier Proteins Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 81:2213-2217 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.81.7.2213 |
| Popis: | Bovine osteogenesis imperfecta is a congenital disease in Holstein cattle having several characteristics in common with human osteogenesis imperfecta syndromes. In particular, affected calves have multiple bone fractures and friable teeth. Bone collagen isolated from the affected animals (Texas variant) showed slightly decreased alpha 1(I) and alpha 2(I) chain electrophoretic mobility and increased hydroxylysine content. Overall collagen was present in the affected bones at 80-90% of normal values. However, osteonectin, a 32,000 Mr bone-specific protein found previously to promote collagen mineralization in vitro and present in abundance (approximately equal to 3% of total protein) in normal calf bone, was severely depleted (less than 2% of normal levels) in the osteogenesis imperfecta bone and dentin. The bone proteoglycan was similarly depleted. In contrast, the bone sialoprotein was not as severely affected. Further, the diseased teeth lacked (less than 10% of normal values) phosphophoryn, a dentin-specific protein normally present as 4-5% of the total calf dentin matrix. The data suggest multiple hard tissue matrix protein deletions, perhaps due to impaired cell development. |
| Databáze: | OpenAIRE |
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